Krause R M, Coligan J E
Rev Infect Dis. 1979 Nov-Dec;1(6):904-11. doi: 10.1093/clinids/1.6.904.
Antibodies to streptococcal carbohydrates have been employed in a number of ways as substitutes for the myeloma proteins in studies of the structures of antibody molecules and the development of the immune response. This review concentrates on the chemical nature of the streptococcal polysaccharides and on structural studies of the variable regions of the light chains of rabbit anitbodies to the group A-variant polysaccharide produced by hyperimmunization. The chemistry of the group A-variant polysaccharide has now been clarified, and this information has explained the frequently reported difficulty in the preparation of precipitating antisera to this antigen. The group A-variant vaccine is a potent antigen, but the bulk of the antibody is nonprecipitating because it is directed against the noreducing terminal sugar of the nonbranched rhamnose polymer. Chemical studies of the light chains of homogeneous rabbit antibodies reveal two hypervariable regions and a J sequence that joins the variable region to the constant region. Although the precise topographic highlights of the antigen-binding site hae yet to be determined, these structural studies have extended our knowledge of the structure and diversity of antibody molecules.
在抗体分子结构及免疫应答发育的研究中,抗链球菌碳水化合物抗体已被以多种方式用作骨髓瘤蛋白的替代品。本综述着重于链球菌多糖的化学性质,以及对经超免疫产生的兔抗A群变异多糖抗体轻链可变区的结构研究。A群变异多糖的化学性质现已阐明,这一信息解释了此前经常报道的针对该抗原制备沉淀抗血清时遇到的困难。A群变异疫苗是一种强效抗原,但大部分抗体不产生沉淀,因为它针对的是无分支鼠李糖聚合物的非还原末端糖。对纯合兔抗体轻链的化学研究揭示了两个高变区以及一个将可变区与恒定区连接起来的J序列。尽管抗原结合位点的确切拓扑特征尚未确定,但这些结构研究扩展了我们对抗体分子结构和多样性的认识。